Ubiquitin found in the archaebacterium <i>Thermoplasma acidophilum</i>

Wolf, Stefan; Lottspeich, Friedrich; Baumeister, Wolfgang

doi:10.1016/0014-5793(93)81757-q

Cited by 45 publications

(21 citation statements)

References 22 publications

(11 reference statements)

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“…At present, the putative posttranslational modification that leads to proteasome-mediated protein degradation in Archaea has not been defined. While some reports suggest the existence of ubiquitin in Archaea (275,300,473), no direct demonstration of archaeal ubiquitin has been provided, nor have analyses of archaeal genomes identified ubiquitin-encoding genes or genes encoding ubiquitin-transferring proteins. Stuctural studies, however, have revealed the existence of ar- (33,375).…”

Section: Protein Ubiquitinationmentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review

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Section: Protein Ubiquitinationmentioning

confidence: 99%

Posttranslational Protein Modification inArchaea

Eichler

Adams

2005

Microbiol Mol Biol Rev

194

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“…Some, but not all, prokaryotes contain Ub (29). The bacterium E. coli lacks Ub but does have an N-end rule pathway ( (9).…”

Section: Figmentioning

confidence: 99%

The N-end rule: functions, mysteries, uses.

Varshavsky

1996

Proc. Natl. Acad. Sci. U.S.A.

787

713

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The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Similar but distinct versions of the N-end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N-end rule pathway is a part of the ubiquitin system. I discuss the mechanisms and functions of this pathway, and consider its applications.The half-lives of proteins in a living cell range from a few seconds to many days. Among the functions of intracellular proteolysis are the elimination of abnormal proteins, the maintenance of amino acid pools in cells affected by stresses such as starvation, and the generation of protein fragments that act as hormones, antigens, or other effectors. Yet another function of proteolytic pathways is selective destruction of proteins whose concentrations must vary with time and alterations in the state of a cell. Metabolic instability is a property of many regulatory proteins. A short in vivo half-lifet of a regulator provides a way to generate its spatial gradients and allows for rapid adjustments of its concentration (or subunit composition) through changes in the rate of its synthesis. Conditionally unstable proteins, long-lived or short-lived depending on the state of a cell, are often deployed as components of control circuits. One example is cyclins-a family of proteins whose destruction at specific stages of the cell cycle regulates cell division and growth (3). In addition, many proteins are long-lived as components of larger complexes such as ribosomes and oligomeric proteins but are metabolically unstable as free sub-

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“…Some, but not all, prokaryotes contain Ub (Wolf et al 1993). The bacterium E. coli lacks Ub but does have an N-end rule pathway (Fig.…”

Section: Figurementioning

confidence: 99%